Linked Life Data

8725902

Source:http://linkedlifedata.com/resource/pubmed/id/8725902

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-12-3
pubmed:abstractText
In the present study, we characterized the epitope of a monoclonal antibody against purified amyloid plaque cores (Am-3). By immunocytochemical experiments, Am-3 stained cerebrovascular and senile plaque amyloid in brain sections of patients with Alzheimer's disease (AD) in a similar manner to that of antibodies against amyloid beta-protein (A beta). By Western blotting experiments, Am-3 recognized only a 35 kDa protein, which was revealed to be glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and not A beta or beta amyloid precursor protein (beta PP). However, Am-3 recognized both GAPDH and purified native A beta in a dot-binding assay. Therefore, we concluded that Am-3 recognized both GAPDH and native A beta. Other monoclonal antibodies (6C6 and AmT-1) against the synthetic peptide corresponding to residues 1-28 of A beta also recognized these proteins. Because the amino acid sequences of these two proteins are not homologous, we propose that the crossreactivity between A beta and GAPDH is a consequence of their similar conformational epitopes. The possibility of crossreactions would complicate immunochemical and immunocytochemical studies of brain aging, AD and Down's syndrome. The implications of crossreactivity in developing immunological assays and in investigating the amyloid deposits of AD are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0197-4580
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
405-14
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Antibodies to amyloid beta protein (A beta) crossreact with glyceraldehyde-3-phosphate dehydrogenase (GAPDH).
pubmed:affiliation
Department of Neurology, University of Tsukuba, Ibaraki, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't